AtDeg2 – a chloroplast protein with dual protease/chaperone activity
The project is supported by grant from Polish National Science Center based on decision DEC-2013/09/B/NZ3/00449
- to perform an in-depth phenotypic screens that interrogate chloroplast functions as well as the general growth and development of the following groups of plants grown under non-stressing conditions: wild type ones, mutants entirely lacking AtDeg2 protein (i.e. exhibiting neither protease nor chaperone AtDeg2 activity), mutants which accumulate a mutated version of AtDeg2 exhibiting a complete loss of protease activity with no effect on chaperone function and to subject the outcomes of the phenotypic screens to a systematic data analysis to reliably identify phenotypic features which are associated with either AtDeg2 protease or its chaperone activity or both
- to identify native protein substrates for AtDeg2 protease activity under stressing conditions (high irradiance)
- to identify native protein substrates for AtDeg2 chaperone activity under stressing conditions (high irradiance)
- to determine which domain of AtDeg2 molecule is responsible for its chaperone activity
The principal aim of the project is to gain a significantly deeper insight into the functional role of AtDeg2 by means of performing the following individual tasks:
Determination of the effect of a point mutation S268A (substitution of serine for alanine in position 268 )
for protease and chaperone activity of chloroplast protein AtDeg2
Student Research Grant founded by the Dean of Faculty of Biology of the Adam Mickiewicz University in Poznań.
Results of the project were presented in June 2016 on the Plant Biology Europe EPSO/FESPB 2016 Congress in Prague.